Eugene Serebryany

@eserebry.bsky.social

Protein mis/folding & engineering, peptides, molecular ophthalmology, chembio | Asst. Prof. Stony Brook University

Proud to share our newest preprint. We introduced conformational constraints (disulfides) into alpha-synclein and measured effects on aggregation. There were surprises, including a possible new amyloid polymorph and a substoichiometric chaperone-like aggregation inhibitor. doi.org/10.64898/202...

Disulfide engineering reveals unexpected pro- and anti-aggregation conformers of human α-synuclein

Intrinsically disordered proteins can aggregate in many distinct conformations (polymorphs). Polymorphs are a striking example of fold-switching: one primary structure able to form distinct tertiary s...

doi.org